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Protein arginine N-methyltransferase 5 (EC 2.1.1.320) (Histone synthetic lethal 7 protein) (Hsl7) (Histone-arginine N-methyltransferase PRMT5)

 ANM5_XENLA              Reviewed;         633 AA.
Q6NUA1;
24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
30-AUG-2017, entry version 70.
RecName: Full=Protein arginine N-methyltransferase 5;
EC=2.1.1.320 {ECO:0000269|PubMed:22009756};
AltName: Full=Histone synthetic lethal 7 protein;
Short=Hsl7;
AltName: Full=Histone-arginine N-methyltransferase PRMT5;
Name=prmt5; Synonyms=hsl7;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH WEE2-A,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15583029; DOI=10.1083/jcb.200406048;
Yamada A., Duffy B., Perry J.A., Kornbluth S.;
"DNA replication checkpoint control of Wee1 stability by vertebrate
Hsl7.";
J. Cell Biol. 167:841-849(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH WDR77, SUBCELLULAR
LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=22009756; DOI=10.1074/jbc.M111.303677;
Wilczek C., Chitta R., Woo E., Shabanowitz J., Chait B.T., Hunt D.F.,
Shechter D.;
"Protein arginine methyltransferase Prmt5-Mep50 methylates histones
H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis
eggs.";
J. Biol. Chem. 286:42221-42231(2011).
[4]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH WDR77 AND
S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, SUBUNIT, AND INTERACTION WITH
WDR77.
PubMed=23451136; DOI=10.1371/journal.pone.0057008;
Ho M.C., Wilczek C., Bonanno J.B., Xing L., Seznec J., Matsui T.,
Carter L.G., Onikubo T., Kumar P.R., Chan M.K., Brenowitz M.,
Cheng R.H., Reimer U., Almo S.C., Shechter D.;
"Structure of the arginine methyltransferase PRMT5-MEP50 reveals a
mechanism for substrate specificity.";
PLoS ONE 8:E57008-E57008(2013).
-!- FUNCTION: Arginine methyltransferase that can both catalyze the
formation of omega-N monomethylarginine (MMA) and symmetrical
dimethylarginine (sDMA), with a preference for the formation of
MMA. Specifically mediates the symmetrical dimethylation of
arginine residues in the small nuclear ribonucleoproteins; such
methylation being required for the assembly and biogenesis of
snRNP core particles. Methylates the arginine in the motif G-R-G-
X-G in its substrates histone H2A, H2AFX and H4, producing both
monomethylated and symmetrically dimethylated 'Arg-3'. Methylates
nucleoplasmin at 'Arg-192', producing both monomethylated and
symmetrically dimethylated 'Arg-192'. Involved in the DNA
replication checkpoint. Promotes entry into mitosis by promoting
the proteasomal degradation of wee2-a. May act as a
transcriptional corepressor in CRY1-mediated repression of the
core circadian component PER1. {ECO:0000269|PubMed:15583029,
ECO:0000269|PubMed:22009756, ECO:0000269|PubMed:23451136}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + [protein]-L-
arginine = 2 S-adenosyl-L-homocysteine + [protein]-
N(omega),N(omega')-dimethyl-L-arginine.
{ECO:0000269|PubMed:22009756}.
-!- SUBUNIT: Heterotetramer; dimer of heterodimer with wdr77.
Interacts with wee2-a; this interaction is disrupted upon
activation of the DNA replication checkpoint.
{ECO:0000269|PubMed:15583029, ECO:0000269|PubMed:22009756,
ECO:0000269|PubMed:23451136}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytosol.
Note=Enriched on chromatin.
-!- TISSUE SPECIFICITY: Detected in egg (at protein level).
{ECO:0000269|PubMed:15583029, ECO:0000269|PubMed:22009756}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
-----------------------------------------------------------------------
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EMBL; AY535008; AAS98802.1; -; mRNA.
EMBL; BC068696; AAH68696.1; -; mRNA.
RefSeq; NP_001084480.1; NM_001091011.1.
UniGene; Xl.46791; -.
PDB; 4G56; X-ray; 2.95 A; A/C=2-633.
PDBsum; 4G56; -.
ProteinModelPortal; Q6NUA1; -.
SMR; Q6NUA1; -.
GeneID; 407754; -.
KEGG; xla:407754; -.
CTD; 407754; -.
Xenbase; XB-GENE-17343549; prmt5.
HOVERGEN; HBG057083; -.
KO; K02516; -.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0034709; C:methylosome; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0090161; P:Golgi ribbon formation; ISS:UniProtKB.
GO; GO:0034969; P:histone arginine methylation; IDA:UniProtKB.
GO; GO:0043985; P:histone H4-R3 methylation; ISS:UniProtKB.
GO; GO:0033314; P:mitotic DNA replication checkpoint; IMP:UniProtKB.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR007857; Arg_MeTrfase_PRMT5.
InterPro; IPR035075; PRMT5.
InterPro; IPR035248; PRMT5_C.
InterPro; IPR035247; PRMT5_TIM.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR10738; PTHR10738; 1.
Pfam; PF05185; PRMT5; 1.
Pfam; PF17286; PRMT5_C; 1.
Pfam; PF17285; PRMT5_TIM; 1.
PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
1: Evidence at protein level;
3D-structure; Biological rhythms; Cell cycle; Cell division;
Chromatin regulator; Cytoplasm; Methyltransferase; Mitosis; Nucleus;
Repressor; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase.
CHAIN 1 633 Protein arginine N-methyltransferase 5.
/FTId=PRO_0000422972.
DOMAIN 304 611 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
REGION 329 330 S-adenosyl-L-methionine binding.
REGION 414 416 S-adenosyl-L-methionine binding.
ACT_SITE 431 431 Proton donor/acceptor. {ECO:0000250}.
ACT_SITE 440 440 Proton donor/acceptor. {ECO:0000250}.
BINDING 300 300 Peptide substrate. {ECO:0000250}.
BINDING 303 303 Peptide substrate. {ECO:0000250}.
BINDING 320 320 S-adenosyl-L-methionine.
BINDING 388 388 S-adenosyl-L-methionine.
BINDING 440 440 S-adenosyl-L-methionine.
STRAND 11 14 {ECO:0000244|PDB:4G56}.
HELIX 21 29 {ECO:0000244|PDB:4G56}.
TURN 30 32 {ECO:0000244|PDB:4G56}.
STRAND 34 41 {ECO:0000244|PDB:4G56}.
STRAND 49 51 {ECO:0000244|PDB:4G56}.
HELIX 54 56 {ECO:0000244|PDB:4G56}.
HELIX 70 75 {ECO:0000244|PDB:4G56}.
STRAND 77 80 {ECO:0000244|PDB:4G56}.
HELIX 92 111 {ECO:0000244|PDB:4G56}.
STRAND 115 120 {ECO:0000244|PDB:4G56}.
HELIX 127 138 {ECO:0000244|PDB:4G56}.
STRAND 145 153 {ECO:0000244|PDB:4G56}.
HELIX 155 158 {ECO:0000244|PDB:4G56}.
HELIX 180 191 {ECO:0000244|PDB:4G56}.
TURN 192 194 {ECO:0000244|PDB:4G56}.
STRAND 198 203 {ECO:0000244|PDB:4G56}.
HELIX 211 217 {ECO:0000244|PDB:4G56}.
STRAND 222 228 {ECO:0000244|PDB:4G56}.
STRAND 231 234 {ECO:0000244|PDB:4G56}.
HELIX 244 254 {ECO:0000244|PDB:4G56}.
TURN 255 257 {ECO:0000244|PDB:4G56}.
STRAND 259 264 {ECO:0000244|PDB:4G56}.
STRAND 269 271 {ECO:0000244|PDB:4G56}.
HELIX 274 284 {ECO:0000244|PDB:4G56}.
STRAND 292 296 {ECO:0000244|PDB:4G56}.
TURN 297 299 {ECO:0000244|PDB:4G56}.
TURN 310 312 {ECO:0000244|PDB:4G56}.
HELIX 317 323 {ECO:0000244|PDB:4G56}.
HELIX 327 344 {ECO:0000244|PDB:4G56}.
TURN 348 352 {ECO:0000244|PDB:4G56}.
STRAND 354 361 {ECO:0000244|PDB:4G56}.
TURN 363 365 {ECO:0000244|PDB:4G56}.
HELIX 366 377 {ECO:0000244|PDB:4G56}.
STRAND 381 389 {ECO:0000244|PDB:4G56}.
HELIX 391 401 {ECO:0000244|PDB:4G56}.
TURN 402 405 {ECO:0000244|PDB:4G56}.
STRAND 409 414 {ECO:0000244|PDB:4G56}.
TURN 416 418 {ECO:0000244|PDB:4G56}.
STRAND 425 430 {ECO:0000244|PDB:4G56}.
HELIX 442 447 {ECO:0000244|PDB:4G56}.
STRAND 453 461 {ECO:0000244|PDB:4G56}.
STRAND 463 472 {ECO:0000244|PDB:4G56}.
HELIX 474 481 {ECO:0000244|PDB:4G56}.
STRAND 486 488 {ECO:0000244|PDB:4G56}.
HELIX 492 495 {ECO:0000244|PDB:4G56}.
HELIX 502 504 {ECO:0000244|PDB:4G56}.
STRAND 505 507 {ECO:0000244|PDB:4G56}.
STRAND 512 520 {ECO:0000244|PDB:4G56}.
STRAND 530 537 {ECO:0000244|PDB:4G56}.
STRAND 542 556 {ECO:0000244|PDB:4G56}.
STRAND 559 562 {ECO:0000244|PDB:4G56}.
STRAND 578 588 {ECO:0000244|PDB:4G56}.
STRAND 593 602 {ECO:0000244|PDB:4G56}.
STRAND 604 613 {ECO:0000244|PDB:4G56}.
STRAND 615 617 {ECO:0000244|PDB:4G56}.
HELIX 624 626 {ECO:0000244|PDB:4G56}.
SEQUENCE 633 AA; 72285 MW; F3A61499DF6623CC CRC64;
MAAGDGGRVS SGRDVACVTE VADTLGAMAN QGFDFLCMPI FHPRFKREFY KEPAKSRPGP
QTRSDLLLSG RDWNTLIVGK LSDWIKTDSE VSRIRKTSEA AMQQELNFSA YLGLPAFLIP
LKQEDNSNLS RLLINHIHVG HHSTMFWMRV PLMAPNDLRD DLIENEPISL SEEDNSGEER
TWIWWHNFRS LCDYNKKIAL AIEIGADLPS GHVIDRWLGE PIKAAFLPTS IFLTNKKGFP
VLTKVHQRLI FKLFKLEVQF VISGSHHHSE KDLCSYLQYL EYLSQNSPPP NAYEMFAKGY
EDYLQSPLQP LMDNLESQTY EVFEKDPVKY SQYQQAVYKC LLDRVPEEEK ETNIQILMVL
GAGRGPLVNA SLRAAKQAER KIKVYAVEKN PNAVITLEGW RYEEWGSQVT VVSGDMREWK
APEKADIIVS ELLGSFGDNE LSPECLDGAQ HFLKDDGVSI PGEYTSYLAP ISSSKLYNEV
RACREKDRDP EAQFEMPYVV RLHNFHQLSD PLPCFTFHHP NKDDVIDNNR YCCLQYRVDL
NTVLHGFAGY FNTVLYKDVT LSICPESHSP GMFSWFPILF PIKQPIPMRE GDTVCVRFWR
CNNGKKVWYE WAVTSPVCSA IHNPTGRSYT IGL


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